AHPC_AMPXN
ID AHPC_AMPXN Reviewed; 188 AA.
AC K0J4Q8; O87200;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2012, sequence version 1.
DT 25-MAY-2022, entry version 48.
DE RecName: Full=Alkyl hydroperoxide reductase C;
DE EC=1.11.1.26 {ECO:0000269|PubMed:10960086};
DE AltName: Full=Peroxiredoxin;
DE AltName: Full=Thioredoxin peroxidase;
GN Name=ahpC; OrderedLocusNames=AXY_22000;
OS Amphibacillus xylanus (strain ATCC 51415 / DSM 6626 / JCM 7361 / LMG 17667
OS / NBRC 15112 / Ep01).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Amphibacillus.
OX NCBI_TaxID=698758;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-13, FUNCTION,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND INDUCTION.
RC STRAIN=ATCC 51415 / DSM 6626 / JCM 7361 / LMG 17667 / NBRC 15112 / Ep01;
RX PubMed=10960086; DOI=10.1128/jb.182.18.5046-5051.2000;
RA Niimura Y., Nishiyama Y., Saito D., Tsuji H., Hidaka M., Miyaji T.,
RA Watanabe T., Massey V.;
RT "A hydrogen peroxide-forming NADH oxidase that functions as an alkyl
RT hydroperoxide reductase in Amphibacillus xylanus.";
RL J. Bacteriol. 182:5046-5051(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51415 / DSM 6626 / JCM 7361 / LMG 17667 / NBRC 15112 / Ep01;
RA Nakazawa H., Katano Y., Nakamura S., Sasagawa M., Fukada J., Arai T.,
RA Sasakura N., Mochizuki D., Hosoyama A., Harada K., Horikawa H., Kato Y.,
RA Harada T., Sasaki K., Sekiguchi M., Hodoyama M., Nishiko R., Narita H.,
RA Hanamaki A., Hata C., Konno Y., Niimura Y., Yamazaki S., Fujita N.;
RT "Whole genome sequence of Amphibacillus xylinus NBRC 15112.";
RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 2-188, AND DISULFIDE BONDS.
RX PubMed=15770647; DOI=10.1002/prot.20412;
RA Kitano K., Kita A., Hakoshima T., Niimura Y., Miki K.;
RT "Crystal structure of decameric peroxiredoxin (AhpC) from Amphibacillus
RT xylanus.";
RL Proteins 59:644-647(2005).
CC -!- FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of
CC hydrogen peroxide and organic hydroperoxides to water and alcohols,
CC respectively. Plays a role in cell protection against oxidative stress
CC by detoxifying peroxides. {ECO:0000269|PubMed:10960086}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a hydroperoxide + H(+) + NADH = an alcohol + H2O + NAD(+);
CC Xref=Rhea:RHEA:62628, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30879, ChEBI:CHEBI:35924, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.11.1.26;
CC Evidence={ECO:0000269|PubMed:10960086};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=8.9 uM for H(2)O(2) {ECO:0000269|PubMed:10960086};
CC KM=10 uM for cumene hydroperoxide {ECO:0000269|PubMed:10960086};
CC -!- SUBUNIT: Homodimer; disulfide-linked, upon oxidation (PubMed:10960086,
CC PubMed:15770647). 5 homodimers assemble to form a ring-like decamer
CC (PubMed:15770647). {ECO:0000269|PubMed:10960086,
CC ECO:0000269|PubMed:15770647}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P0AE08}.
CC -!- INDUCTION: Induced significantly under aerobic conditions.
CC {ECO:0000269|PubMed:10960086}.
CC -!- MISCELLANEOUS: The active site is a conserved redox-active cysteine
CC residue, the peroxidatic cysteine (C(P)), which makes the nucleophilic
CC attack on the peroxide substrate. The peroxide oxidizes the C(P)-SH to
CC cysteine sulfenic acid (C(P)-SOH), which then reacts with another
CC cysteine residue, the resolving cysteine (C(R)), to form a disulfide
CC bridge. The disulfide is subsequently reduced by an appropriate
CC electron donor to complete the catalytic cycle. In this typical 2-Cys
CC peroxiredoxin, C(R) is provided by the other dimeric subunit to form an
CC intersubunit disulfide (PubMed:15770647). The disulfide is subsequently
CC reduced by AhpF (By similarity). {ECO:0000250|UniProtKB:P0A251,
CC ECO:0000305|PubMed:15770647}.
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily.
CC {ECO:0000305}.
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DR EMBL; AB018435; BAA33808.1; -; Genomic_DNA.
DR EMBL; AP012050; BAM48332.1; -; Genomic_DNA.
DR RefSeq; WP_015010915.1; NC_018704.1.
DR PDB; 1WE0; X-ray; 2.90 A; A/B/C/D/E/F/G/H/I/J=2-188.
DR PDBsum; 1WE0; -.
DR AlphaFoldDB; K0J4Q8; -.
DR SMR; K0J4Q8; -.
DR STRING; 698758.AXY_22000; -.
DR PeroxiBase; 4918; AxAhpC.
DR EnsemblBacteria; BAM48332; BAM48332; AXY_22000.
DR KEGG; axl:AXY_22000; -.
DR PATRIC; fig|698758.3.peg.2211; -.
DR eggNOG; COG0450; Bacteria.
DR HOGENOM; CLU_042529_21_3_9; -.
DR OMA; FWYPKDF; -.
DR OrthoDB; 892697at2; -.
DR Proteomes; UP000006294; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0102039; F:alkylhydroperoxide reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR GO; GO:0051920; F:peroxiredoxin activity; IEA:InterPro.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR InterPro; IPR017559; AhpC.
DR InterPro; IPR000866; AhpC/TSA.
DR InterPro; IPR024706; Peroxiredoxin_AhpC-typ.
DR InterPro; IPR019479; Peroxiredoxin_C.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR10681:SF121; PTHR10681:SF121; 1.
DR Pfam; PF10417; 1-cysPrx_C; 1.
DR Pfam; PF00578; AhpC-TSA; 1.
DR PIRSF; PIRSF000239; AHPC; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR TIGRFAMs; TIGR03137; AhpC; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antioxidant; Cytoplasm; Direct protein sequencing;
KW Disulfide bond; Oxidoreductase; Peroxidase; Redox-active center;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:10960086"
FT CHAIN 2..188
FT /note="Alkyl hydroperoxide reductase C"
FT /id="PRO_0000441069"
FT DOMAIN 2..158
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT ACT_SITE 48
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000305|PubMed:15770647"
FT DISULFID 48
FT /note="Interchain (with C-167); in linked form"
FT /evidence="ECO:0000269|PubMed:15770647,
FT ECO:0007744|PDB:1WE0"
FT DISULFID 167
FT /note="Interchain (with C-48); in linked form"
FT /evidence="ECO:0000269|PubMed:15770647,
FT ECO:0007744|PDB:1WE0"
FT STRAND 12..16
FT /evidence="ECO:0007829|PDB:1WE0"
FT STRAND 18..20
FT /evidence="ECO:0007829|PDB:1WE0"
FT STRAND 23..26
FT /evidence="ECO:0007829|PDB:1WE0"
FT TURN 27..30
FT /evidence="ECO:0007829|PDB:1WE0"
FT STRAND 31..39
FT /evidence="ECO:0007829|PDB:1WE0"
FT HELIX 50..64
FT /evidence="ECO:0007829|PDB:1WE0"
FT STRAND 67..75
FT /evidence="ECO:0007829|PDB:1WE0"
FT HELIX 77..85
FT /evidence="ECO:0007829|PDB:1WE0"
FT HELIX 88..91
FT /evidence="ECO:0007829|PDB:1WE0"
FT STRAND 95..99
FT /evidence="ECO:0007829|PDB:1WE0"
FT HELIX 104..108
FT /evidence="ECO:0007829|PDB:1WE0"
FT TURN 114..117
FT /evidence="ECO:0007829|PDB:1WE0"
FT STRAND 121..126
FT /evidence="ECO:0007829|PDB:1WE0"
FT STRAND 130..138
FT /evidence="ECO:0007829|PDB:1WE0"
FT HELIX 148..160
FT /evidence="ECO:0007829|PDB:1WE0"
SQ SEQUENCE 188 AA; 20774 MW; E61BA53C0215BA84 CRC64;
MSLIGTEVQP FRAQAFQSGK DFFEVTEADL KGKWSIVVFY PADFSFVCPT ELEDVQKEYA
ELKKLGVEVY SVSTDTHFVH KAWHENSPAV GSIEYIMIGD PSQTISRQFD VLNEETGLAD
RGTFIIDPDG VIQAIEINAD GIGRDASTLI NKVKAAQYVR ENPGEVCPAK WEEGGETLKP
SLDIVGKI
